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The bromodomain interaction module.

Panagis Filippakopoulos1, Stefan Knapp

  • 1Nuffield Department of Clinical Medicine, Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7LD, UK. panagis.filippakopoulos@sgc.ox.ac.uk

FEBS Letters
|June 20, 2012
PubMed
Summary
This summary is machine-generated.

ε-N-acetylation of lysine residues (K(ac)) is a key post-translation modification. Bromodomains (BRDs) recognize these sites, offering potential for new therapeutic strategies targeting protein interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • ε-N-acetylation of lysine residues (K(ac)) is a prevalent post-translation modification (PTM) in the human proteome.
  • Nuclear histone acetylation is linked to transcriptional activation, but the functions of most acetylation events remain unclear.
  • Bromodomains (BRDs) are protein modules that specifically recognize K(ac) sites.

Purpose of the Study:

  • To provide an overview of bromodomain sequence requirements.
  • To summarize known bromodomain substrates.
  • To elucidate the structural mechanisms of K(ac) recognition by bromodomains.

Main Methods:

  • Literature review of bromodomain research.
  • Analysis of sequence data for bromodomain recognition motifs.
  • Structural analysis of bromodomain-K(ac) interactions.

Main Results:

  • Detailed sequence requirements for bromodomain binding have been identified.
  • A range of protein substrates for bromodomains have been cataloged.
  • Structural insights into the specific recognition of K(ac) by bromodomains are presented.

Conclusions:

  • Bromodomains are crucial readers of the acetylation code.
  • Understanding BRD-K(ac) interactions is vital for deciphering cellular signaling.
  • Targeting bromodomains offers a promising avenue for novel therapeutic interventions.